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Information on EC 1.2.1.8 - betaine-aldehyde dehydrogenase and Organism(s) Oryza sativa and UniProt Accession Q84LK3

for references in articles please use BRENDA:EC1.2.1.8
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IUBMB Comments
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) . In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
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This record set is specific for:
Oryza sativa
UNIPROT: Q84LK3
Word Map
The taxonomic range for the selected organisms is: Oryza sativa
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
betaine aldehyde dehydrogenase, badh2, pabadh, osbadh2, badh1, betaine-aldehyde dehydrogenase, osbadh1, betaine aldehyde dehydrogenase 2, badh2-e7, pkbadh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
BADH1
BADH2
badh2-E2
284081
recessive allele, truncated form, with a 7-bp deletion in exon 2 (82 residues)
badh2-E7
284082
recessive allele, truncated form (251 amino acid polypeptide)
betaine aldehyde dehydrogenase
betaine aldehyde dehydrogenase 1
1975
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betaine aldehyde dehydrogenase 2
1975
-
betaine aldehyde oxidase
-
-
-
0
betaine aldehyde:NAD(P)+ oxidoreductase
1975
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dehydrogenase, betaine aldehyde
-
-
-
0
OsALDH10-1
284070
-
OsALDH10-2
284071
-
OsBADH1
284070
-
OsBADH2
284071
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
betaine aldehyde + NAD+ + H2O = betaine + NADH + 2 H+
show the reaction diagram
the enzyme catalyzes the second step of the two-step conversion of choline into glycine betaine
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
0
oxidation
reduction
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-
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0
SYSTEMATIC NAME
IUBMB Comments
betaine-aldehyde:NAD+ oxidoreductase
In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase) [5]. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
9028-90-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
the appropriate level of glycine may be regulated at both the transcriptional and posttranscriptional levels; namely, the transcription is induced abundantly in response to the osmotic stresses, while the proper amount of precise gene products is balanced by posttranscriptional processing
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ir
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
show the reaction diagram
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
3-aminopropionaldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
3-dimethylsulfoniopropionaldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
3-N-trimethylaminopropionaldehyde + NAD+ + H2O
3-N-trimethylaminopropionate + NADH + H+
show the reaction diagram
-
-
-
-
?
4-aminobutanal + NAD+ + H2O
4-aminobutanoate + NADH
show the reaction diagram
-
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
show the reaction diagram
-
-
-
-
?
4-gamma-aminobutyraldehyde + NAD+ + H2O
?
show the reaction diagram
-
-
-
-
?
4-N-trimethylaminobutyraldehyde + NAD+ + H2O
4-N-trimethylaminobutyrate + NADH + H+
show the reaction diagram
-
-
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
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-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
-
the appropriate level of glycine may be regulated at both the transcriptional and posttranscriptional levels; namely, the transcription is induced abundantly in response to the osmotic stresses, while the proper amount of precise gene products is balanced by posttranscriptional processing
-
ir
3-aminopropionaldehyde + NAD+ + H2O
3-aminopropionate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyrate + NADH + H+
show the reaction diagram
-
-
-
?
4-aminobutyraldehyde + NAD+ + H2O
4-aminobutyric acid + NADH + H+
show the reaction diagram
-
-
-
-
?
betaine aldehyde + NAD+ + H2O
betaine + NADH + H+
show the reaction diagram
belongs to the NAD-dependent dehydrogenase family, characterized by the typical aldehyde substrate binding domain
-
-
?
betaine aldehyde + NAD+ + H2O
glycine betaine + NADH + H+
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
0.5 M, expression of OsBADH2 is increased under salt stress conditions, but at high concentrations, expression is inhibited.
NaCl
0.5 M, firstly, expression of OsBADH1 is increased under salt stress conditions, but at high concentrations, expression has been inhibited.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NaCl
expression of OsBADH2 gene is low without salt stress and increased under salt stress conditions. A high ion concentration (0.5 M) inhibited trancription of the gene
NaCl
expression of OsBADH1 gene was very low without salt stress and increased under salt stress conditions. However, a high ion concentration (0.5 M) inhibited trancription of this gene
additional information
-
salt stress, BADH1
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0012 - 0.017
3-aminopropionaldehyde
0.035 - 0.34
3-N-trimethylaminopropionaldehyde
0.0078 - 0.041
4-N-trimethylaminobutyraldehyde
0.13 - 0.17
acetaldehyde
0.23 - 2.6
Betaine aldehyde
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
source for isolating the total RNA
Manually annotated by BRENDA team
source for isolating the total RNA
Manually annotated by BRENDA team
source for isolating the totl RNA
Manually annotated by BRENDA team
source for isolating the total RNA
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
-
betaine aldehyde dehydrogenase 2 is a key enzyme in the synthesis of fragrance aroma compounds. The extremely low activity of the enzyme in catalyzing the oxidation of acetaldehyde is crucial for the accumulation of the volatile compound 2-acetyl-1-pyrroline in fragrant rice
physiological function
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
side-chain modification Attention: controlled vocabulary for this datafield
commentary
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch method, in the presence of NAD+, using 0.1 M HEPES pH 7.4, 24% (w/v) PEG 4000 and 0.2 M ammonium chloride
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni Sepharose affinity column chromatography, and gel filtration
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using nickel-nitrilotriacetic acid agarose affinity chromatography columns after expression in E. coli
using nickel-nitrilotriacetic acid agarose affinity chromatography columns after expression in Escherichia coli
using nickel-nitrilotriacetic acid agarose after cloning and expression in Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
For OsBADH2, preliminary experiments based on RT-PCR show that the mRNA is expressed constitutively and multiple transcription products ae detected. Primers specific to the 5' region are used. To analyze the transcripts derived from the OsBADH2 gene, seedlings from different varieties under different rowth conditions are harvested for the total RNA isolation. As a result, all the 59 cDNA clones sequenced also have deletions at the 5' exonic region. Similar to that in the OsBADH1 gene, various unusual events in the OsBADH2 locus generate a number of truncated transcripts. The size of the deleted sequences from 5' UTR and exon(s) range from 112 to 523 nucleotides.
into the pGEM-T easy vector for sequencing
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli strain BL21
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in Escherichia coli strain BL21 (DE3)
into the pGEM-T easy vector for sequencing
to examine whether the expressed products are OsBADh1 gene, the RT-PCR-amplified fragments are cloned and sequenced. Primers derived from 5' and 3' untranslated regions are used to isolate the full length of OsBADH1 cDNA clones. Resultant sequencing analysis reveal that the cDNAs are truncated at the 5' exonic region. Observed expression products are shorter than the expected size of 695 bp of the 5' exonic region. Sequence comparison of the cDNAs reveal a considerable variation in their structural compositions. All of the cDNAs contain a deletion of the 5' coding sequence within the OsBADH1 gene. The deleted exon material ranged from 28 to 225 nucleotides in size. The start-point of the deletions in four cDNAs begin with the first nucleotide of the coding sequence, which give rise to the loss of translation initiation codon. 32 cDNAs encode derivatives with frame-shifts in the open reading frame , introducing various stop codons at different positions. Only 5 cDNA clones show the potential to encode partial BADH1 proteins with deletions that code for a part of the putative NAD+ binding domain. Most of the missing sequences from the truncated transcripts indicate above involved 2 different exons, and in a few cases the truncation take place within a single exon. In addition, two independent deletions of exon materials within a single cDNA clone are observed in 5 clones. Therefore, no cDNA is found to have the capacity to encode the full length of the OsBADH1 protein, indicating that correctly processed transcripts represent a very small proportion of the total cytoplasmic mature OsBADH1 RNA population and consequently that the majority of the OsBADH1 mRNAs are unlikely to encode functional proteins.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of isozymes BADH1 and BADH2 is decreased by the submerged treatment and recovered to control (0 h) level after re-aeration
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, S.; Yang, Y.; Shi, W.; Ji, Q.; He, F.; Zhang, Z.; Cheng, Z.; Liu, X.; Xu, M.
Badh2, encoding betaine aldehyde dehydrogenase, inhibits the biosynthesis of 2-scetyl-1-pyrroline, a major component in rice fragrance
Plant Cell
20
1850-1861
2008
Oryza sativa (B3VMC0), Oryza sativa (B3VMC1), Oryza sativa (B3VMC2), Oryza sativa
Manually annotated by BRENDA team
Niu, X.; Zheng, W.; Lu, B.R.; Ren, G.; Huang, W.; Wang, S.; Liu, J.; Tang, Z.; Luo, D.; Wang, Y.; Liu, Y.
An unusual posttranscriptional processing in two betaine aldehyde dehydrogenase loci of cereal crops directed by short, direct repeats in response to stress conditions
Plant Physiol.
143
1929-1942
2007
Solanum lycopersicum, Triticum aestivum, Triticum aestivum (Q8LGQ9), Oryza sativa (O24174), Oryza sativa (Q84LK3), Oryza sativa, Spinacia oleracea (P17202), Spinacia oleracea, Zea mays (Q53CF4), Zea mays, Hordeum vulgare (Q94IC0), Hordeum vulgare (Q94IC1), Hordeum vulgare, Arabidopsis thaliana (Q9S795), Arabidopsis thaliana (Q9STS1)
Manually annotated by BRENDA team
Gao, C.; Han, B.
Evolutionary and expression study of the aldehyde dehydrogenase (ALDH) gene superfamily in rice (Oryza sativa)
Gene
431
86-94
2009
Oryza sativa (O24174), Oryza sativa (Q84LK3)
Manually annotated by BRENDA team
Fitzgerald, T.L.; Waters, D.L.; Henry, R.J.
Betaine aldehyde dehydrogenase in plants
Plant Biol.
11
119-130
2009
Avena sativa, Beta vulgaris, Embryophyta, Hordeum vulgare, Oryza sativa, Pisum sativum, Zoysia tenuifolia
Manually annotated by BRENDA team
Sakthivel, K.; Sundaram, R.M.; Shobha Rani, N.; Balachandran, S.M.; Neeraja, C.N.
Genetic and molecular basis of fragrance in rice
Biotechnol. Adv.
27
468-473
2009
Oryza sativa
Manually annotated by BRENDA team
Mitsuya, S.; Yokota, Y.; Fujiwara, T.; Mori, N.; Takabe, T.
OsBADH1 is possibly involved in acetaldehyde oxidation in rice plant peroxisomes
FEBS Lett.
583
3625-3629
2009
Oryza sativa
Manually annotated by BRENDA team
Kovach, M.J.; Calingacion, M.N.; Fitzgerald, M.A.; McCouch, S.R.
The origin and evolution of fragrance in rice (Oryza sativa L.)
Proc. Natl. Acad. Sci. USA
106
14444-14449
2009
Oryza sativa
Manually annotated by BRENDA team
Kuaprasert, B.; Silprasit, K.; Horata, N.; Khunrae, P.; Wongpanya, R.; Boonyalai, N.; Vanavichit, A.; Choowongkomon, K.
Purification, crystallization and preliminary X-ray analysis of recombinant betaine aldehyde dehydrogenase 2 (OsBADH2), a protein involved in jasmine aroma, from Thai fragrant rice (Oryza sativa L.)
Acta Crystallogr. Sect. F
67
1221-1223
2011
Oryza sativa
Manually annotated by BRENDA team
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